ID   Q4L509_STAHJ            Unreviewed;       602 AA.
AC   Q4L509;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   OrderedLocusNames=SH1957 {ECO:0000313|EMBL:BAE05266.1};
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808 {ECO:0000313|EMBL:BAE05266.1, ECO:0000313|Proteomes:UP000000543};
RN   [1] {ECO:0000313|EMBL:BAE05266.1, ECO:0000313|Proteomes:UP000000543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435 {ECO:0000313|EMBL:BAE05266.1,
RC   ECO:0000313|Proteomes:UP000000543};
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- FUNCTION: Has oligopeptidase activity and degrades a variety of small
CC       bioactive peptides. {ECO:0000256|RuleBase:RU368091}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU368091};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU368091};
CC   -!- SIMILARITY: Belongs to the peptidase M3B family.
CC       {ECO:0000256|RuleBase:RU368091}.
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DR   EMBL; AP006716; BAE05266.1; -; Genomic_DNA.
DR   RefSeq; WP_011276227.1; NC_007168.1.
DR   AlphaFoldDB; Q4L509; -.
DR   GeneID; 58061929; -.
DR   KEGG; sha:SH1957; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_2_0_9; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000000543; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09608; M3B_PepF; 1.
DR   Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR   Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR   Gene3D; 1.10.287.830; putative peptidase helix hairpin domain like; 1.
DR   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR004438; Peptidase_M3B.
DR   NCBIfam; TIGR00181; pepF; 1.
DR   PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   Pfam; PF08439; Peptidase_M3_N; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368091};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368091};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU368091};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU368091};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          117..186
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          207..587
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   602 AA;  70002 MW;  399EDD3AE8C0BED9 CRC64;
     MSQQLTREEQ ERKYPNDTWD LTTIFKNDEA FEEALKEVEG YLGKEEQFKG HLADSADTLC
     DALALEDEIG TKLEKVYVYA HLKQDQDTSN DKYTGFESRA HQLIIKISSA WSFLVPEILQ
     IDEDKLQSFI ETNDNLKRYE FDLKLINEKR PHILDAEQER LLTEAQDALS TPSNVYGMFS
     NADLEFEDAV DKDGEKHPLT QGTFIKYLES DDRELRQSAY NNLYKAYGAY NNTLGSTLAG
     EVKKNVFNAR THNYKTARER ALSNNHIPEE VYDNLVKTVH KYLPLLHRYT KLRKELLAVD
     ELKMYDLYTP MVKDVKFEMP YEEAKEWMLK ALEPMGEEYL DVVKEGLNNR WVDVYENKGK
     RSGGYSSGAH LTNPFILLNW SDTVSDLYTL IHEFGHSAHS YFSRKHQPSN SSDYSIFVAE
     VASTCNEALL SDYMDKHLDD ERRLLLLNQE LERFRATLFR QTMFAEFEHK IHQIEEAGEP
     LTATRMNDEY AKLNKQYFGD VVETDDNISK EWSRIPHFYM NYYVYQYATG YSAAQSLSHQ
     ILTEGKPAVE RYINEFLKKG SSNYPIEILK NAGVDMTSPE PIEQACEVFE QKLDTFEKLM
     KA
//